PKSC_BACSU
ID PKSC_BACSU Reviewed; 288 AA.
AC O34825;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Polyketide biosynthesis malonyl CoA-acyl carrier protein transacylase PksC;
DE Short=AT;
DE EC=2.3.1.39;
GN Name=pksC; OrderedLocusNames=BSU17100;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=16757561; DOI=10.1073/pnas.0603148103;
RA Calderone C.T., Kowtoniuk W.E., Kelleher N.L., Walsh C.T., Dorrestein P.C.;
RT "Convergence of isoprene and polyketide biosynthetic machinery: isoprenyl-
RT S-carrier proteins in the pksX pathway of Bacillus subtilis.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:8977-8982(2006).
RN [3]
RP SUBCELLULAR LOCATION.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=17190806; DOI=10.1073/pnas.0609073103;
RA Straight P.D., Fischbach M.A., Walsh C.T., Rudner D.Z., Kolter R.;
RT "A singular enzymatic megacomplex from Bacillus subtilis.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:305-310(2007).
RN [4]
RP FUNCTION IN BACILLAENE BIOSYNTHESIS.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=17234808; DOI=10.1073/pnas.0610503104;
RA Butcher R.A., Schroeder F.C., Fischbach M.A., Straight P.D., Kolter R.,
RA Walsh C.T., Clardy J.;
RT "The identification of bacillaene, the product of the PksX megacomplex in
RT Bacillus subtilis.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1506-1509(2007).
CC -!- FUNCTION: Involved in some intermediate steps for the synthesis of the
CC antibiotic polyketide bacillaene which is involved in secondary
CC metabolism. It catalyzes the transfer of the malonyl-CoA group to the
CC acyl-carrier-protein AcpK (Mal-AcpK). {ECO:0000269|PubMed:16757561,
CC ECO:0000269|PubMed:17234808}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=holo-[ACP] + malonyl-CoA = CoA + malonyl-[ACP];
CC Xref=Rhea:RHEA:41792, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:78449; EC=2.3.1.39;
CC Evidence={ECO:0000269|PubMed:16757561};
CC -!- PATHWAY: Antibiotic biosynthesis; bacillaene biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17190806}.
CC -!- SIMILARITY: Belongs to the FabD family. {ECO:0000305}.
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DR EMBL; AL009126; CAB13582.1; -; Genomic_DNA.
DR PIR; A69678; A69678.
DR RefSeq; NP_389591.1; NC_000964.3.
DR RefSeq; WP_003231821.1; NZ_JNCM01000035.1.
DR PDB; 5DZ6; X-ray; 1.44 A; A=1-288.
DR PDBsum; 5DZ6; -.
DR AlphaFoldDB; O34825; -.
DR SMR; O34825; -.
DR STRING; 224308.BSU17100; -.
DR PaxDb; O34825; -.
DR PRIDE; O34825; -.
DR EnsemblBacteria; CAB13582; CAB13582; BSU_17100.
DR GeneID; 939504; -.
DR KEGG; bsu:BSU17100; -.
DR PATRIC; fig|224308.179.peg.1853; -.
DR eggNOG; COG0331; Bacteria.
DR InParanoid; O34825; -.
DR OMA; LNKTQFT; -.
DR PhylomeDB; O34825; -.
DR BioCyc; BSUB:BSU17100-MON; -.
DR UniPathway; UPA01003; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004314; F:[acyl-carrier-protein] S-malonyltransferase activity; IBA:GO_Central.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.40.366.10; -; 1.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR024925; Malonyl_CoA-ACP_transAc.
DR InterPro; IPR004410; Malonyl_CoA-ACP_transAc_FabD.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR PIRSF; PIRSF000446; Mct; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SUPFAM; SSF52151; SSF52151; 1.
DR SUPFAM; SSF55048; SSF55048; 1.
DR TIGRFAMs; TIGR00128; fabD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Antibiotic biosynthesis; Cytoplasm;
KW Reference proteome; Transferase.
FT CHAIN 1..288
FT /note="Polyketide biosynthesis malonyl CoA-acyl carrier
FT protein transacylase PksC"
FT /id="PRO_0000388004"
FT ACT_SITE 87
FT /evidence="ECO:0000250"
FT ACT_SITE 193
FT /evidence="ECO:0000250"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:5DZ6"
FT TURN 14..19
FT /evidence="ECO:0007829|PDB:5DZ6"
FT HELIX 20..23
FT /evidence="ECO:0007829|PDB:5DZ6"
FT HELIX 25..35
FT /evidence="ECO:0007829|PDB:5DZ6"
FT HELIX 39..45
FT /evidence="ECO:0007829|PDB:5DZ6"
FT HELIX 47..52
FT /evidence="ECO:0007829|PDB:5DZ6"
FT HELIX 54..76
FT /evidence="ECO:0007829|PDB:5DZ6"
FT STRAND 81..86
FT /evidence="ECO:0007829|PDB:5DZ6"
FT HELIX 89..96
FT /evidence="ECO:0007829|PDB:5DZ6"
FT HELIX 102..117
FT /evidence="ECO:0007829|PDB:5DZ6"
FT STRAND 121..129
FT /evidence="ECO:0007829|PDB:5DZ6"
FT HELIX 132..141
FT /evidence="ECO:0007829|PDB:5DZ6"
FT STRAND 147..154
FT /evidence="ECO:0007829|PDB:5DZ6"
FT STRAND 157..163
FT /evidence="ECO:0007829|PDB:5DZ6"
FT HELIX 164..175
FT /evidence="ECO:0007829|PDB:5DZ6"
FT STRAND 182..185
FT /evidence="ECO:0007829|PDB:5DZ6"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:5DZ6"
FT HELIX 198..208
FT /evidence="ECO:0007829|PDB:5DZ6"
FT TURN 223..225
FT /evidence="ECO:0007829|PDB:5DZ6"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:5DZ6"
FT HELIX 231..233
FT /evidence="ECO:0007829|PDB:5DZ6"
FT HELIX 234..240
FT /evidence="ECO:0007829|PDB:5DZ6"
FT HELIX 241..243
FT /evidence="ECO:0007829|PDB:5DZ6"
FT HELIX 248..256
FT /evidence="ECO:0007829|PDB:5DZ6"
FT STRAND 262..265
FT /evidence="ECO:0007829|PDB:5DZ6"
FT STRAND 267..270
FT /evidence="ECO:0007829|PDB:5DZ6"
FT HELIX 271..284
FT /evidence="ECO:0007829|PDB:5DZ6"
SQ SEQUENCE 288 AA; 32464 MW; AFAE397EAB2FD3C6 CRC64;
MITYVFPGQG SQKQGMGSGL FDEFKELTDQ ADEILGYSIK RLCLENPYSN LNKTQFTQPA
LYVVNALSYL KKIRDEEVKP DFVAGHSLGE YNALFAAEAF DFETGLQLVR KRGELMSLIS
NGGMAAVMGL NEEQVAKALK EYHLHDVDIA NVNAPYQIVI SGKKDEIEKA ASLFETMTEV
TMVLPLNVSG AFHSRYMNKA KEEFEEFLHA FYFSPPSIPV ISNVYAKPYT YEFMKQTLAD
QINHSVKWTD SISYLMKKGH MEFEEVGPGN VLTGLIHRIK KDAEAMPR
